ID A0A0Q7MXE7_9NOCA Unreviewed; 368 AA.
AC A0A0Q7MXE7;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=Ferredoxin {ECO:0000313|EMBL:KQY31990.1};
GN ORFNames=ASD42_20265 {ECO:0000313|EMBL:KQY31990.1};
OS Nocardia sp. Root136.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Nocardia.
OX NCBI_TaxID=1736458 {ECO:0000313|EMBL:KQY31990.1, ECO:0000313|Proteomes:UP000051507};
RN [1] {ECO:0000313|Proteomes:UP000051507}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root136 {ECO:0000313|Proteomes:UP000051507};
RA Garrido-Oter R., Bai Y.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQY31990.1, ECO:0000313|Proteomes:UP000051507}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root136 {ECO:0000313|EMBL:KQY31990.1,
RC ECO:0000313|Proteomes:UP000051507};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KQY31990.1}.
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DR EMBL; LMFE01000009; KQY31990.1; -; Genomic_DNA.
DR RefSeq; WP_056820655.1; NZ_LMFE01000009.1.
DR AlphaFoldDB; A0A0Q7MXE7; -.
DR STRING; 1736458.ASD42_20265; -.
DR Proteomes; UP000051507; Unassembled WGS sequence.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR CDD; cd00207; fer2; 1.
DR CDD; cd06185; PDR_like; 1.
DR Gene3D; 3.10.20.30; -; 1.
DR Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1.
DR Gene3D; 2.40.30.10; Translation factors; 1.
DR InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR InterPro; IPR012675; Beta-grasp_dom_sf.
DR InterPro; IPR008333; Cbr1-like_FAD-bd_dom.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR PANTHER; PTHR47354:SF1; CARNITINE MONOOXYGENASE REDUCTASE SUBUNIT; 1.
DR PANTHER; PTHR47354; NADH OXIDOREDUCTASE HCR; 1.
DR Pfam; PF00970; FAD_binding_6; 1.
DR Pfam; PF00111; Fer2; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR PRINTS; PR00409; PHDIOXRDTASE.
DR SUPFAM; SSF54292; 2Fe-2S ferredoxin-like; 1.
DR SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR PROSITE; PS51085; 2FE2S_FER_2; 1.
DR PROSITE; PS51384; FAD_FR; 1.
PE 4: Predicted;
KW 2Fe-2S {ECO:0000256|ARBA:ARBA00022714};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022714}.
FT DOMAIN 52..156
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT DOMAIN 284..368
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
SQ SEQUENCE 368 AA; 39486 MW; 365C9551B4FBC6D4 CRC64;
MTVYPAPTVI PPDLYGKHEH DPTTRVLDTV ANLRVRWSTL INRRPLLTRA DDARFPVVVT
DRALVAEDQA VLSLGLRAPD GAQLPRWAPG AHIDIELPSG RLRQYSLCGD PAETGEYRIA
VRRIPHGGGG SIEIHDELTV GTAVVIRGPR NAFPFAPPGR GSSAKRLHFV AGGIGITPIL
AMARAADRLG IAWTLVYCGR SRDTLPFLDE LAELRGHVVV RTDDEHGTPG AADILDGVDH
DTAIYCCGPT PMTAVLIAAV RTMPGIEFHS ERFSPAPVVD GTAFEVELTS TGEVIAVGAD
QTMLDALLAV RPDQPYSCRQ GFCRTCVVRV TDGTPDHRDG ALTPEEHAAG VTLACVSRCA
GKRLVLDL
//
